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8HDK

Structure of the Rat GluN1-GluN2C NMDA receptor in complex with glycine and glutamate (minor class in symmetry)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005216molecular_functionmonoatomic ion channel activity
A0006811biological_processmonoatomic ion transport
A0015276molecular_functionligand-gated monoatomic ion channel activity
A0016020cellular_componentmembrane
A0038023molecular_functionsignaling receptor activity
B0005216molecular_functionmonoatomic ion channel activity
B0006811biological_processmonoatomic ion transport
B0015276molecular_functionligand-gated monoatomic ion channel activity
B0016020cellular_componentmembrane
B0038023molecular_functionsignaling receptor activity
C0005216molecular_functionmonoatomic ion channel activity
C0006811biological_processmonoatomic ion transport
C0015276molecular_functionligand-gated monoatomic ion channel activity
C0016020cellular_componentmembrane
C0038023molecular_functionsignaling receptor activity
D0005216molecular_functionmonoatomic ion channel activity
D0006811biological_processmonoatomic ion transport
D0015276molecular_functionligand-gated monoatomic ion channel activity
D0016020cellular_componentmembrane
D0038023molecular_functionsignaling receptor activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1068
DetailsTOPO_DOM: Extracellular => ECO:0000250|UniProtKB:Q00960
ChainResidueDetails
BARG20-ALA554
DARG20-ALA554

site_idSWS_FT_FI2
Number of Residues66
DetailsTRANSMEM: Helical => ECO:0000250|UniProtKB:Q00960
ChainResidueDetails
BVAL555-MET573
BMET628-TYR643
DVAL555-MET573
DMET628-TYR643

site_idSWS_FT_FI3
Number of Residues64
DetailsTOPO_DOM: Cytoplasmic => ECO:0000250|UniProtKB:Q00960
ChainResidueDetails
BPHE574-GLY600
BARG621-ILE627
DPHE574-GLY600
DARG621-ILE627

site_idSWS_FT_FI4
Number of Residues38
DetailsINTRAMEM: Discontinuously helical => ECO:0000250|UniProtKB:Q00960
ChainResidueDetails
BLYS601-PRO620
DLYS601-PRO620

site_idSWS_FT_FI5
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q00959
ChainResidueDetails
BSER509
BARG516
BSER687
DSER509
DARG516
DSER687

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q00960
ChainResidueDetails
BTHR511
BASP729
DTHR511
DASP729
CSER688
CASP732

site_idSWS_FT_FI7
Number of Residues2
DetailsSITE: Functional determinant of NMDA receptors => ECO:0000250
ChainResidueDetails
BASN612
DASN612
CASN61
CASN239

site_idSWS_FT_FI8
Number of Residues12
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BASN70
DASN438
DASN539
DASN685
BASN73
BASN337
BASN438
BASN539
BASN685
DASN70
DASN73
DASN337

site_idSWS_FT_FI9
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:24876489, ECO:0007744|PDB:3Q41, ECO:0007744|PDB:4PE5
ChainResidueDetails
AASN276
CASN276

site_idSWS_FT_FI10
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:24876489, ECO:0007744|PDB:4PE5
ChainResidueDetails
AASN300
CASN300

site_idSWS_FT_FI11
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0007744|PubMed:24090084
ChainResidueDetails
AASN350
AASN771
CASN350
CASN771

site_idSWS_FT_FI12
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:24876489, ECO:0007744|PDB:4PE5, ECO:0007744|PubMed:24090084
ChainResidueDetails
AASN440
CASN440

site_idSWS_FT_FI13
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN471
AASN491
AASN674
CASN471
CASN491
CASN674

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PDB entries from 2024-07-24

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